Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2006 |
| Outros Autores: | , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| Texto Completo: | http://hdl.handle.net/10362/82925 |
Resumo: | The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 Å resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 Å. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer. |
| id |
RCAP_fb21320a484757de66f8b1cfbac5a88c |
|---|---|
| oai_identifier_str |
oai:run.unl.pt:10362/82925 |
| network_acronym_str |
RCAP |
| network_name_str |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| repository_id_str |
https://opendoar.ac.uk/repository/7160 |
| spelling |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenboroughnitrate reductase (cytochrome)protein subunitcytochrome a1cytochrome c1membrane proteinnitrate reductaseBiophysicsStructural BiologyBiochemistryGeneticsCondensed Matter PhysicsThe cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 Å resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 Å. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNRodrigues, M. L.Oliveira, T.Matias, P. M.Martins, I. C.Valente, FilipaPereira, I. A.C.Archer, M.2019-10-01T22:40:21Z2006-06-012006-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article4application/pdfhttp://hdl.handle.net/10362/82925eng1744-3091PURE: 14581536http://www.scopus.com/inward/record.url?scp=33745129677&partnerID=8YFLogxKhttps://doi.org/10.1107/S1744309106016629info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-22T17:41:20Zoai:run.unl.pt:10362/82925Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T17:12:32.799003Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
| dc.title.none.fl_str_mv |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| title |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| spellingShingle |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough Rodrigues, M. L. nitrate reductase (cytochrome) protein subunit cytochrome a1 cytochrome c1 membrane protein nitrate reductase Biophysics Structural Biology Biochemistry Genetics Condensed Matter Physics |
| title_short |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| title_full |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| title_fullStr |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| title_full_unstemmed |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| title_sort |
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough |
| author |
Rodrigues, M. L. |
| author_facet |
Rodrigues, M. L. Oliveira, T. Matias, P. M. Martins, I. C. Valente, Filipa Pereira, I. A.C. Archer, M. |
| author_role |
author |
| author2 |
Oliveira, T. Matias, P. M. Martins, I. C. Valente, Filipa Pereira, I. A.C. Archer, M. |
| author2_role |
author author author author author author |
| dc.contributor.none.fl_str_mv |
Instituto de Tecnologia Química e Biológica António Xavier (ITQB) RUN |
| dc.contributor.author.fl_str_mv |
Rodrigues, M. L. Oliveira, T. Matias, P. M. Martins, I. C. Valente, Filipa Pereira, I. A.C. Archer, M. |
| dc.subject.por.fl_str_mv |
nitrate reductase (cytochrome) protein subunit cytochrome a1 cytochrome c1 membrane protein nitrate reductase Biophysics Structural Biology Biochemistry Genetics Condensed Matter Physics |
| topic |
nitrate reductase (cytochrome) protein subunit cytochrome a1 cytochrome c1 membrane protein nitrate reductase Biophysics Structural Biology Biochemistry Genetics Condensed Matter Physics |
| description |
The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 Å resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 Å. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer. |
| publishDate |
2006 |
| dc.date.none.fl_str_mv |
2006-06-01 2006-06-01T00:00:00Z 2019-10-01T22:40:21Z |
| dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
| dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/82925 |
| url |
http://hdl.handle.net/10362/82925 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
1744-3091 PURE: 14581536 http://www.scopus.com/inward/record.url?scp=33745129677&partnerID=8YFLogxK https://doi.org/10.1107/S1744309106016629 |
| dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
4 application/pdf |
| dc.source.none.fl_str_mv |
reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia instacron:RCAAP |
| instname_str |
FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia |
| instacron_str |
RCAAP |
| institution |
RCAAP |
| reponame_str |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| collection |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| repository.name.fl_str_mv |
Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia |
| repository.mail.fl_str_mv |
info@rcaap.pt |
| _version_ |
1833596520433188864 |